Y018_CLOB1
ID Y018_CLOB1 Reviewed; 893 AA.
AC A7FQ49;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=UPF0182 protein CLB_0018 {ECO:0000255|HAMAP-Rule:MF_01600};
GN OrderedLocusNames=CLB_0018;
OS Clostridium botulinum (strain ATCC 19397 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441770;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19397 / Type A;
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01600};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01600}.
CC -!- SIMILARITY: Belongs to the UPF0182 family. {ECO:0000255|HAMAP-
CC Rule:MF_01600}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000726; ABS33718.1; -; Genomic_DNA.
DR RefSeq; WP_011947903.1; NC_009697.1.
DR AlphaFoldDB; A7FQ49; -.
DR SMR; A7FQ49; -.
DR GeneID; 5184266; -.
DR KEGG; cba:CLB_0018; -.
DR HOGENOM; CLU_007733_0_0_9; -.
DR OMA; HLRYPQD; -.
DR OrthoDB; 170146at2; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR HAMAP; MF_01600; UPF0182; 1.
DR InterPro; IPR005372; UPF0182.
DR PANTHER; PTHR39344; PTHR39344; 1.
DR Pfam; PF03699; UPF0182; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Transmembrane; Transmembrane helix.
FT CHAIN 1..893
FT /note="UPF0182 protein CLB_0018"
FT /id="PRO_0000335540"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01600"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01600"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01600"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01600"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01600"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01600"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01600"
SQ SEQUENCE 893 AA; 104057 MW; 373E2697913CBAFB CRC64;
MKNKKALFIP LFIIILFIAF FNKIINFIIN IKWFKEVNYL AVYFTKMRAI IILMIPIFII
FFISIWMYYK SLIINKNKSV VDIGLNKNNY GKKLFFIFNF IVSIFLAYIF SSSYWYRILQ
FNNSVDFNVK DPIFFKDVSF YIFKLPLFES LYKVIISLLL FLVITTFIAY FILEAKYKIQ
SKKDINLKNI NHGIKSFAGK QLAIVSGLII LFISFGHLIK IWNLVYSSNG VSFGASYTDV
HATLLFYKII VVITLISSIV TLLSIVKGKF KPVSICIGIT IFLIVSQNIA SFLVQNFIVK
SNEKTLEQPY IKNNIDLTRK AFALDDIEIR DFDIKNDLQK QDITDNKASI DNIRINSFKP
TLEFYNQVQI IRYYYTFNDI DIDRYNINGK YNQVFLAARE IDTDALNPNT WQNRHLIYTH
GFGAVMNKVN SVTSEGQPDF VIKDIPPYNK TNIKLANPRI YFGEKTNDYV IVNTKINEFD
YPKEDSNKTN KYNGHAGIKM SFINRLLFAI NKKDINFLLS KDIKKDSKII INRNIVERAK
KIAPFLTYDS DPYMVIYNGK IYWIIDAYTT TNRYPYSEPY DSINYIRNSA KVVIDSVDGD
INFYITDKKD PIVNNYAKIF KGLFKEEKDA PKEIREHFRY PKDLFSIQSK VLGKYHVKDP
GVFYNGEDLW EVSKDQKHVE GETNTNDAPY IIMKLPDQNK EEMVLLNYFN VMKKDNMIAL
FGARMDGEQY GKKILYKLPS DKTVYSPYLF KQKINQDTNI SKELSLWNRE GSKVQYGDTI
ILPIKNSLLY IEPLYLRASG KNSIPEMKRV ILSYNDKLVL SSSIQEGIKE IFNSKDNKIN
DKNEKDSTKT IDDSKLKKAQ EYYNKAIEAQ KNGDWTKYGE NINELGNILN SIK